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Database: UniProt
Entry: A0A139I4L2_9PEZI
LinkDB: A0A139I4L2_9PEZI
Original site: A0A139I4L2_9PEZI 
ID   A0A139I4L2_9PEZI        Unreviewed;      2180 AA.
AC   A0A139I4L2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC579_2844 {ECO:0000313|EMBL:KXT09525.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT09525.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT09525.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT09525.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT09525.1}.
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DR   EMBL; LFZO01000331; KXT09525.1; -; Genomic_DNA.
DR   STRING; 113226.A0A139I4L2; -.
DR   Proteomes; UP000073492; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          369..801
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1677..1754
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1813..1890
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1656..1679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1757..1807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2180 AA;  235653 MW;  57912B5E42409AE0 CRC64;
     MSNILLFGDQ TAEQYPLLRK VALHKDNVLV HNFVQRCALA LREEARALPR TQRLLIPDFL
     TVNNLIEAYY QKGDKVPALE SALLTIAQLG HYIGYFSEHP SELPAASNTR VLALCTGLLA
     AAAVVSSKTI DELVSLGVEF VRVAFRSGAA VDGIRSVLGQ TGEEKEPWST IVTGVNAASA
     KKALDAFHKE KDIPHSNQAY ISAVSVMAIT ISGPPTTVER FFHDGPLSQN NRVPIPIYGP
     YHAEHLYNDA DIERLLSGKV ARELRSHTPA SLVHSAATGK PFVAENSYEL AKLALGEMLQ
     RPVRWDYLLE ETVPQMAASK QGAKIYAMGV SNTANSLVSA LKAGGQTNVS VIDQSAFVEQ
     QGYNGRTQND KIAIVGMAGR YPNSANHEAL WDLLIKGLDV HRKIPADRFD ADAHCDPSGK
     GKNKSHTPYG CFIDEPGLFD PRFFNMSPRE AAQTDPMGRL ALVTAYEALE MSGYVPNRTP
     STKLHRIGTF YGQTSDDWRE INAAENVDTY FITGGVRAFA PGRINYYFKF SGPSYSVDTA
     CSSSLAAIQL ACTSLWAGDC DTACAGGLNV LTNPDIFSGL SKGQFLSKTG SCKTYDNAAD
     GYCRGDACGT VILKRYQDAI ADKDNILGCI LGAATNHSAE AVSITHPHAG AQEFLYKQVL
     ANAGVDAHEI SYVEMHGTGT QAGDGIEMTS VTNVFAPRHR QRRPEQTVHL GAIKANVGHA
     EAASGINSLH KVLLMMKHDK IPANVGIKGE MNKTFPADLK DRNVHISRDA VSWPRKGAEP
     RKVFLNNFSA AGGNTALLIE DGPMRDAPAE VDPRSTLPVT VTARSIASLK RNLVNLQQYM
     IENPGTTATS FSYTTTARRI QHNYRVAFPL ADMNKVIDSI QAQIKESYNP VPMAATKTAF
     CFTGQGSQYT GLGQKLYQDL KSFRDDINQL DQLARVQGLP SFLELLDGTD VQTLSPVKVQ
     LGMACIQVAL ARMWSSWGII PTAVIGHSLG EYAALHVAGV ISAADMVLLV GRRAELLVRD
     CTPHTHGMLA VKGSAEAIRA TLGSKMTEIA CINGPEETVL CGSGDVVASA NDTLTRRGFK
     ATKLNVPFAF HSAQVDPILD QFKRIASSVT FNKPTVPVLS PLAGEIIREA GVIGPDYLAR
     HARETVNFWT ALTSGQKAKV FDEKTAWLEV GAHPVCSGMV KASIGATVTA PSLRRGEDAW
     KTIATSVCQL FMAGVYVNFD EYHREFNDAQ ELLQLPTYSF DNKKYWLDYH NNWTLRKGEP
     AEVREVVVEK AVAQPVPAVE IPAKRLSTSC QKVISEEFTD NQAKVVVRSS LADSKLYPVV
     CGHMVNNAAL CPSSLYADMA LTLGDYIWKE MRPGTEAPGL NVCNMEVPKP FIAQIPQPAQ
     GQHIELEANA DLEQGIVKLQ FRSVQPDGKK ILDHAHCIVR FEEKAAWADE WARYNFMVKA
     QIDLLTAKTM NGGAHKVQRG MAYKLFKALV NYEGKYRAMS EVVLDGQNTE ASATLDFPTK
     PEDGDFYCPP YHIDGSCHIS GFIVNASDLL DSEQNVYVSH GWGAMKFSKP LTAGMKLRNY
     VRMLPQPNNI SKGDVYILEG DEIVAVCEGI KFQQIPRRVL NTFLPPNKGS AARPAAVAAP
     VKSSPVRAAA PAPIKVAPSP AAVRAPAPAP IKIAAPAPAP ASAPKPAKPK KAPAPRKASG
     GLVDKVMKIL AKETEVDTSE LVDDAQFENL GVDSLLSLTI SAIFREELDM EISSSLFTDN
     ATVGDMKKYF AQFDNGSVSS ASEPDEDSED ESIPATDMPT PLDMLSTPAS SAPSVAASDA
     GKPELDSPVR DSLAEVGDVS LARHVVAQEM GVDLSEITDD AELAELGMDS LMSLTILGEL
     REKTGVDLPS TFLSSNPTIK DIEDALAEIN KTDISRYPPA TSVLLQGNAK VATKKLFFLP
     DGSGSATSYV SIPNLGPDVA AYGLNCPFMK DPEQWQCGIE VSSLIYLAEI KRRQPKGPYI
     IGGWSAGGVI AYAVAQALLA AGEKVSKLLL LDSPCPVNLD PLPSRLHIFF NEIGLLGTGD
     PSKTPKWLLP HFSAAIRSLS AYDPKPSIAD LPTFAVWCTD GVAGNPGDPR PPPAEDEDPA
     PMKWLLNHRT DFADNGWAQL CQGSFKNGIM AGHHFSMMKD PHAADLGKLI RAGLDWDGKR
     ESAATVHVSG SIRKGYTPPA
//
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